ArticleJournal of biotechnology2012
Structure-guided engineering of Lactococcus lactis alcohol dehydrogenase LlAdhA for improved conversion of isobutyraldehyde to isobutanol.
Article in Journal of biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 41 citations in OpenAlex.
- Substrate expansion of Geotrichum candidum alcohol dehydrogenase towards diaryl ketones by mutation.Applied microbiology and biotechnology · 2024Article
- Engineering new-to-nature biochemical conversions by combining fermentative metabolism with respiratory modules.Nature communications · 2024Article
- Engineering the carbon and redox metabolism of Paenibacillus polymyxa for efficient isobutanol production.Microbial biotechnology · 2024Article
- Growth-coupled anaerobic production of isobutanol from glucose in minimal medium with Escherichia coli.Biotechnology for biofuels and bioproducts · 2023Article
- Isobutanol production by combinedMetabolic engineering communications · 2022Article
- Comparative functional genomics identifies an iron-limited bottleneck in aSynthetic and systems biotechnology · 2022Article
- Modulating redox metabolism to improve isobutanol production in Shimwellia blattae.Biotechnology for biofuels · 2021Article
- Article
- Mutations in adenine-binding pockets enhance catalytic properties of NAD(P)H-dependent enzymes.Protein engineering, design & selection : PEDS · 2016Article
- Combinatorial application of two aldehyde oxidoreductases on isobutanol production in the presence of furfural.Journal of industrial microbiology & biotechnology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
We have determined the X-ray crystal structures of the NADH-dependent alcohol dehydrogenase LlAdhA from Lactococcus lactis and its laboratory-evolved variant LlAdhA(RE1) at 1.9Å and 2.5Å resolution, respectively. LlAdhA(RE1), which contains three amino acid mutations (Y50F, I212T, and L264V), was engineered to increase the microbial production of isobutanol (2-methylpropan-1-ol) from isobutyraldehyde (2-methylpropanal). Structural comparison of LlAdhA and LlAdhA(RE1) indicates that the enhanced activity on isobutyraldehyde stems from increases in the protein's active site size, hydrophobicity, and substrate access. Further structure-guided mutagenesis generated a quadruple mutant (Y50F/N110S/I212T/L264V), whose KM for isobutyraldehyde is ∼17-fold lower and catalytic efficiency (kcat/KM) is ∼160-fold higher than wild-type LlAdhA. Combining detailed structural information and directed evolution, we have achieved significant improvements in non-native alcohol dehydrogenase activity that will facilitate the production of next-generation fuels such as isobutanol from renewable resources.
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